Papilla formation during sporulation by synchronized minicycle cells of the fungus Blastocladiella emersonii provides a model system for the study of the synthesis and extracellular transport of glycoprotein. It involves the vectorial transport of both an amorphous glycoprotein to form a papilla plug and hydrolytic enzymes to degrade the preexisting cell wall in that localized region. The papilla plugs will be isolated and their structural components analyzed chemically; particular emphasis will be placed on characterization of the carbohydrate and protein moeities of the major glycoprotein. Biosynthesis of the papilla glycoprotein and required hydrolytic enzymes (chitinase, and perhaps protease and/or glucanase) will be studied by means of pulse labeling and cell fractionation experiments in conjunction with inhibitors of synthesis and exocytosis. The steps in the synthesis and transport of glycoprotein and chitinase, the initation and coordination of these events in papilla formation and the requirement for new papilla-specific glycosyl transferases will be examined. A hypothesis will be tested that predicts the coordinated, stage-specific transport of the required factors to the localized wall region by a single secretory vesicle system. The co-transport of the papilla glycoprotein and cell wall-lytic enzymes will be examined by isolation and analysis of the secretory vesicles that give rise to the papilla via exocytosis.